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2024 SEM 1 CYTOGENETICS > the central dogma > Flashcards

the central dogma Flashcards

1
Q

this help to break into amino acids

A

digestive enzymes
(amylase, protease, lipase,lactase, sucrase, maltase)

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2
Q

where do the amino acids enter after it has broken down by the digestive enzymes

A

bloodstream through the interior lining of the small intestine
and into the cells, where RNA molecules transcribed from genes guide their assembly into new proteins

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3
Q

nonessential -
conditionally essential -
essential -

A

nonessential - 5
body can produce on its own
no need to get from diet
Alanine
Asparagine
Aspartate
Glutamate
Serine

conditionally essential - 6
body can make them but if have illness or stress (metabolic disease) body may not produce enough
Arginine
Cysteine
Glutamine
Glycine
Proline
Tyrosine

essential -6
cannot be made by the body
get from food/ diet
Phenylalanine
Histidine
Isoleucine
Leucine
Lysine
Methionine
Threonine
Tryptophan
Valine

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4
Q

what is the structure of the amino acid

A

central carbon atom bonded
- hydrogen atom
- amino grp, NH2
- acid grp, COOH
- R group

*link via peptide bond

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5
Q

a protein that consists of one or more long chains of amino acids

A

polypeptides

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6
Q

shorter chains of amino acids

A

peptides

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7
Q

a protein’s three-dimensional shape

A

conformation

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8
Q

it is described the relationship between nucleic acids and proteins as a directional flow of information

A

called the central dogma
discovered by:
James Watson and Francis Crick
- their structure of DNA in 1953

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9
Q

differences and similarities of dna and rna

A

index card

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10
Q

The bases of an RNA sequence are complementary to those of one strand of the double helix

A

template strand

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11
Q

it is the non template strand of the DNA double helix

A

coding strand

*the coding region
- contains the sequence of codons
- carries the genetic info for translation

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12
Q

an enzyme that builds and RNA molecule

A

RNA polymerase

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13
Q

dna polymerase vs rna polymerase

A

index card

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14
Q

types of RNA (size)
- function

A

messenger RNA (500 - 4,500)
- encodes aa sequences

ribosomal RNA (100 - 300)
- associates w proteins = form ribosomes
- support and catalyze protein synthesis

translate RNA (75 - 80)
- transport specific aa to the ribosomes for protein synthesis

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15
Q

where does the rRNA found

A

in the ribosomes
“cell’s protein making machine”

-catalyze formation of peptide bonds between amino acids

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16
Q

ribosomes structure

A

large subunit (3 molecule)
- aka in eukaryotes: 60S subunits
- 5347 rna base
-47 proteins
- catalyze the formation of peptide bonds btwn aa

small subunit (1molecule)
- aka if in eukaryotes: 40S subunit (svedberg unit)
- 1869 rna base
- 32 proteins
- responsible for reading the mRNA during translation
-ensure that correct tRNA pairs with mRNA codons

*the ribosomes have 2 separate subunits in cytoplasm but they join at the site of the chain initiation

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17
Q

tRNA structure

A

index card

  • tRNAs will bring in more amino acids to the dna
  • connect one by one = form chain until stop signal
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18
Q

it is the protein that help control which gene to turn on or off

A

transcription factors
has a specific areas of thhe transcription factors called the binding domains

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19
Q

what are the different type of domains

A

helix-turn-helix:
twisted spiral, followed by a bend, and then another spiral.

zinc fingers:
resemble a “finger” that grabs the DNA, and they often need zinc (a metal) to hold their shape.

leucine zippers:
look like a zipper, with leucine (an amino acid) acting like the teeth of the zipper that help the transcription factor hold onto the DNA

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20
Q

steps of transcription

A

initiation:
rna polymerase attach to dna at the promoter
starts unwinding the DNA strand so it can read the gene
*promoter serves as the starting point

elongation:
RNA polymerase moves along the DNA strand
reading its sequence and building an RNA strand by adding complementary RNA bases (A, U, C, G

termination:
RNA polymerase reaches the terminator sequence (a “stop” signal) = stops transcription
made RNA is released, and RNA polymerase detaches from the DNA

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21
Q

help RNA polymerase find where to start on the DNA

A

transcription factors

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22
Q

flow of RNA processing

A

transcription:
cell makes a rough copy (pre-mRNA) of the DNA strand
copy includes everything - both the important parts (exons) and the unnecessary parts (introns)

modification:
cap” at the front end (5’ end) - like putting a protective cover on the beginning
“tail” at the back end (3’ end) made of many A’s - like adding a protective backing

splicing:
mRNA
cuts out introns
keeps exons
joins exons tgt

enzymes proofread the remaining RNA

final product:
mature mRNA
moves out the nucleus into the cytoplasm
- can be used to make proteins

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23
Q

what are the 4 genetic code

A
  1. the code is triplet
    dna & rna uses 3-letter code called codon
  2. the code does not overlap
    code is read straight through in groups of three, without overlap
    example: AUGCCCAAG is read as AUG-CCC-AAG (like reading word-by-word)

3.the code includes control
start” and “stop” signals built into the code
stop: UGA, UAA, and UAG
start: AUG

4.the code is same in all species
all living things (from bacteria to humans) use the same genetic code
different three-letter combinations can code for the same amino acid (synonymous codons)

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24
Q

what is the minimum no. of bases in a codon

A

3

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25
Q

how many does the genetic code cld specify 20 amino acids

A

64 different three-letter combinations to specify 20 amino acids

26
Q

codons that termed different amino acids

A

nonsynonymous codons

27
Q

different codon that specify the same amino acids

A

synonymous codons

28
Q

the first amino acids in the protein chain

A

Met, methionine

29
Q

terminating translation

A

ppt slide

30
Q

where does translation take place

A

on free ribosomes in the cytoplasm
associated with the endoplasmic reticulum - make and transport proteins

31
Q

after protein is made, how many times does the protein fold into

A

one or more conformations
- it folds to the right shape to function properly

32
Q

it stabilize partially folded regions in their correct form, and prevent a protein from getting “stuck” in a useless intermediate form

A

chaperone proteins
- help guide folding process, fold into correct shapes and don’t get stuck in the middle of folding

33
Q

what happens when a protein is folded incorrectly (misfolded)

A

a system called unfolded protein response kicks in
slow or stops the protein synthesis
while increasing the production of more chaperone proteins and other folding proteins to fix the problem.

34
Q

it is when the misfolded proteins are sent out of the ER back into the cytoplasm, where they are “tagged” with yet another protein

A

ubiquitin

  • If a protein gets one ubiquitin tag, it might be able to unfold and refold correctly.
35
Q

what happens to the misfolded protein bearing

one ubiquitin tag:

more than one ubiquitin tag:

A

one ubiquitin tag:
straighten and refold correctly

more than one ubiquitin tag:
taken to another cellular machine called a proteasome
whr it breaks down into peptides to amino acids = reuse

36
Q

what are the two ways that the proteins misfold

A

mutation:
change the aa sequences
alters attractions and repulsions

having more than one conformation:
proteins fold into more than 1 shape =
cant work properly
cause problems

37
Q

what are the type of disease when proteins misfold and cant do their jobs properly

A

Alzheimer disease
Familial amyotrophic lateral sclerosis
frontotemporal dementia
Heredity ATTR amyloidosis
Parkinson disease
Lewy body dementia
PKU
Prion disease

38
Q

what happens when one conformation becomes “infectious”

A

it converts molecules with other conformations into more copies of itself

  • basically cause other proteins of the same kind to fold into this harmful shape. It’s like a bad influence that makes healthy proteins change into a harmful form.
39
Q

this is called the “infectious proteins”

A

prion disease
- subgrp of protein misfolding
sheep > scrapie
proteinaceous infectious agents

40
Q

proteins that can misfold and cause other proteins to misfold in a harmful way, leading to serious diseases.

A

prions

41
Q

what is the first step in dna replication

A

unzip the dna
helicase breaks the hydrogen bonds of the bases into 2 strands

42
Q

it attaches the primers to single strand

A

primase

43
Q

function of dna polymerase

A

can only add new nucleotides in the 5’ to 3’ direction

44
Q

what are the fragments called in the lagging strand

A

okazaki fragments
hence need ligase to connect those together

45
Q

functions of proteins

A

blood clotting
muscle contractions
antibodies/ immunoglobulins
hair/ skin/ connective tissue
enzymes- important for biochemical functions

46
Q

where do these process occur in the cell
replication:
transcription:
translation:

A

replication: nucleus (“S” phase)
transcription: nucleus
translation: cytoplasm (ribosomes)

47
Q

this RNA encodes amino acid sequence

A

mRNA

48
Q

this RNA associates with proteins to form ribosomes, which structurally support and catalyze protein synthesis

A

rRNA

49
Q

this RNA transport specific amino acids to the ribosomes for protein synthesis

A

tRNA

50
Q

when do the large and small subunit come together

A

both come tgt during translation to form a complete ribosome

51
Q

it is a sequence that binds a complementary mRNA codon

A

anticodon

52
Q

what is the function of the transcription factor

A

binds DNA at certain sequence
initiates transcription of specific site on chromosomes

*essential in initiation and regulation

53
Q

it provides binding site for transcription factors and rna polymerase

A

promoters

54
Q

this is the first transcription factor and a binding protein that recognizes the TATA regions and bind to DNA

A

TATA binding protein

55
Q

what happens after rna polymerase is attached to the promoter

A

rna polymerase will unwind small portion of dna

56
Q

directionality in
transcription:
synthesis:

A

transcription:
3’ to 5’ on a dna template strand

synthesis:
synthesis of mRNA in a 5’ to 3’ direction

57
Q

what are the modifications made in the pre-mRNA

A

addition of the
5’ mRNA cap - modified guanine
helps protect RNA
help ribosomes recognize mRNA

3’ poly A tail - abt 200 adenine
stability

afterwards it will undergo splicing (spliceosomes)

remove the non coding regions, introns and combine coding regions, exons

it will then exit out of the nucleus to find ribosomes to undergo translation

58
Q

what type of energy is used in the translation process

A

ATP:
initiation

GTP:
elongation
termination

59
Q

one example of quaternary structure of a protein

A

hemoglobin

60
Q

this protein stabilize partially folded regions in their correct form and prevent a protein from getting stuck in a useless intermediate form

A

chaperone

61
Q

CTFR protein

A

The CFTR protein is like a little gate that controls salt and water flow in our cells. This helps keep mucus thin, so it can clear out easily, especially in the lungs.

Chaperone proteins are like helpers that make sure CFTR folds into the right shape so it can work properly. If CFTR doesn’t fold right, it can’t reach the cell’s surface, leading to thick mucus, which causes problems in conditions like cystic fibrosis.

2024 SEM 1 CYTOGENETICS (11 decks)

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